1byh
From Proteopedia
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MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE
Overview
The three-dimensional structure of the hybrid Bacillus, 1,3-1,4-beta-glucanase (beta-glucanase; 1,3-1,4-beta-D-glucan, 4-glucanohydrolase, lichenase, EC 3.2.1.73) designated H(A16-M) was, determined by x-ray crystallography at a resolution of 2.0 A and refined, to an R value of 16.4% using stereochemical restraints. The protein, molecule consists mainly of two seven-stranded antiparallel beta-pleated, sheets arranged atop each other to form a compact, sandwich-like, structure. A channel crossing one side of the protein molecule, accommodates an inhibitor, 3,4-epoxybutyl beta-D-cellobioside, which binds, covalently to the side chain of Glu-105, as seen in a crystal structure, analysis at 2.8-A resolution of the protein-inhibitor complex (R = 16.8%)., That Glu-105 may be indispensible for enzyme catalysis by H(A16-M) is, suggested by site-directed mutagenesis of this residue, which inevitably, leads to an inactive enzyme.
About this Structure
1BYH is a Single protein structure of sequence from Synthetic construct with CA and NBU as ligands. Active as Licheninase, with EC number 3.2.1.73 Full crystallographic information is available from OCA.
Reference
Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase., Keitel T, Simon O, Borriss R, Heinemann U, Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5287-91. PMID:8099449
Page seeded by OCA on Tue Nov 20 12:01:36 2007
Categories: Licheninase | Single protein | Synthetic construct | Heinemann, U. | Keitel, T. | CA | NBU | Hydrolase
